The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement

Metcalfe R, Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M
Journal of Biological Chemistry :jbc.RA119.012351 (2020 Apr 24)

doi: 10.1074/jbc.RA119.012351
Submitted to SASBDB: 2019 Jul 24
Published in SASBDB:

SASDGG2 – Interleukin 11 receptor subunit alpha

Interleukin-11 receptor subunit alpha experimental SAS data
PDB model
Sample: Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
RgGuinier 3.0 nm
Dmax 9.5 nm
VolumePorod 41 nm3

SASDGH2 – Interleukin 11, N-terminally truncated

Interleukin 11, N-terminal truncation experimental SAS data
PDB model
Sample: Interleukin 11, N-terminal truncation monomer, 18 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
RgGuinier 1.7 nm
Dmax 5.4 nm
VolumePorod 22 nm3

SASDGJ2 – Interleukin 11, full length

Interleukin 11 experimental SAS data
PDB model
Sample: Interleukin 11 monomer, 19 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
RgGuinier 1.9 nm
Dmax 6.1 nm
VolumePorod 28 nm3

SASDGK2 – Interleukin 11/Interleukin 11 receptor alpha complex

Interleukin-11 receptor subunit alphaInterleukin 11, N-terminal truncation experimental SAS data
OTHER model
Sample: Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein
Interleukin 11, N-terminal truncation monomer, 18 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
RgGuinier 3.3 nm
Dmax 10.2 nm
VolumePorod 84 nm3